[HTML][HTML] Biochemical and structural investigations clarify the substrate selectivity of the 2-oxoglutarate oxygenase JMJD6
JmjC domain-containing protein 6 (JMJD6) is a 2-oxoglutarate (2OG)-dependent oxygenase
linked to various cellular processes, including splicing regulation, histone modification,
transcriptional pause release, hypoxia sensing, and cancer. JMJD6 is reported to catalyze
hydroxylation of lysine residue (s) of histones, the tumor-suppressor protein p53, and
splicing regulatory proteins, including u2 small nuclear ribonucleoprotein auxiliary factor 65-
kDa subunit (U2AF65). JMJD6 is also reported to catalyze N-demethylation of N-methylated …
linked to various cellular processes, including splicing regulation, histone modification,
transcriptional pause release, hypoxia sensing, and cancer. JMJD6 is reported to catalyze
hydroxylation of lysine residue (s) of histones, the tumor-suppressor protein p53, and
splicing regulatory proteins, including u2 small nuclear ribonucleoprotein auxiliary factor 65-
kDa subunit (U2AF65). JMJD6 is also reported to catalyze N-demethylation of N-methylated …